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Related Experiment Videos

[Proteolysis directed by the extracellular matrix].

William Hornebeck1, Hervé Emonard, François-Xavier Maquart

  • 1FRE 2534 CNRS-IFR 53 Biomolécules, Faculté de Médecine, 51 rue Cognacq Jay, 51095 Reims, France. william.hornebeck@univ-reims.fr

Journal De La Societe De Biologie
|July 19, 2003
PubMed
Summary

Extracellular matrix (ECM) degradation involves plasminogen and matrix metalloproteinase (MMP) systems. Matricellular proteins like thrombospondins may offer therapeutic strategies to control cell invasion by regulating MMPs.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Context:

  • Extracellular matrix (ECM) degradation is crucial in physio-pathological processes.
  • Proteolytic systems, including the plasmin(ogen) system and matrix metalloproteinases (MMPs), drive ECM breakdown.
  • Enzyme activity occurs via proteolytic cascades in the pericellular environment, involving protein assemblies on specialized cell membrane structures.

Purpose:

  • To elucidate the mechanisms of ECM degradation by proteolytic systems.
  • To explore the role of MMPs and their products (matricryptins, matrikins) in modulating gene expression.
  • To investigate the interaction between matrix components, gelatinases, and matricellular proteins.

Summary:

  • ECM degradation relies on plasminogen and MMP systems, forming proteolytic cascades.

Related Experiment Videos

  • MMP activity generates peptides that modulate MMP expression and activate growth factors like TGF-beta.
  • Matricellular proteins, such as thrombospondins 1 and 2, regulate gelatinase A activity, influencing cell invasion.

    • Impact:

    • Understanding these proteolytic systems and their regulation is key to controlling pathological cell invasion.
    • Matrikins and pseudo-matrikins show therapeutic potential for targeting cell invasion.
    • This research highlights novel therapeutic targets for diseases involving excessive ECM degradation and cell motility.